In Streptococcus pneumoniae, heat shock induces the synthesis of 65-, 73-, and 84-kDa proteins, and ethanol shock induces a 104-kDa protein. In this study, the 65-, 84-, and 104-kDa proteins were identified as members of the GroEL, CIpL and alcohol dehydrogenase families, respectively, and the general properties of the stress response of S. pneumoniae to several other stresses were characterized. However, several stresses which are known to induce stress responses in Escherichia coli and Bacillus subtilis failed to induce any high molecular weight heat-shock proteins (HSPs) such as GroEL and DnaK homologues. A minor temperature shift from 30 to 37 C triggered induction of the homologues of DnaK and GroEL of E. coli. These features may provide a foundation for evaluating the role of heat-shock proteins relative to the physiology and pathogenesis of pneumococcus.

Streptococcus pneumoniae was isolated from patients with bacteremia, meningitis, pneumonia, and otitis media and used to determine susceptibility to various antibiotics. Of 105 isolates, 51% to 83% were resistant to 6 antibiotics (i.e., the percentages of resistance to penicillin, ampicillin, cephalothin, chloramphenicol, tetracycline, and erythromycin were 78%, 67%, 51%, 56%, 83%, and 58%, respectively). Also, 66 of the 105 isolates were multidrug resistant. Seventy-eight percent of multidrug-resistant strains were highly resistant to tetracycline (minimum inhibitory concentration [MIC] > or = 50 micrograms/ml), and 39% of multidrug-resistant strains were also highly resistant to erythromycin (MIC > or = 128 micrograms/ml). However, only 4% of the 105 isolates were resistant to cefotaxime.

In Streptococcus pneumoniae, heat shock induces the synthesis of 65-, 73-, and 84-kDa proteins, and ethanol shock induces a 104-kDa protein. In this study, the 65-, 84-, and 104-kDa proteins were identified as members of the GroEL, CIpL and alcohol dehydrogenase families, respectively, and the general properties of the stress response of S. pneumoniae to several other stresses were characterized. However, several stresses which are known to induce stress responses in Escherichia coli and Bacillus subtilis failed to induce any high molecular weight heat-shock proteins (HSPs) such as GroEL and DnaK homologues. A minor temperature shift from 30 to 37 C triggered induction of the homologues of DnaK and GroEL of E. coli. These features may provide a foundation for evaluating the role of heat-shock proteins relative to the physiology and pathogenesis of pneumococcus.

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